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236 Anatomy-Chemistry
Building
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The goal of the research is to gain a detailed understanding at the molecular and physical chemical level of how proteins bind and recognize other proteins, drugs, ligands and nucleic acids. Theoretical and computational methods used include Poisson-Boltzmann electrostatics, Molecular and Browian Dynamics, and Monte Carlo simulations. Current Research:
Selected Publications: Sharp, K. (2001) Entropy-enthalpy compensation: fact or artifact? Protein Sci. 10:661-667. Prabhu, N. V., S.D. Dalosto, K.A. Sharp, W.W. Wright and J.M. Vanderkooi (2002) Optical spectra of Fe(II) cytochrome c interpreted using molecular dynamics simulations and quantum mechanical calculations. J. Phys. Chem. 106:5561-5571. Luo, H. and K.A. Sharp (2002).
On the calculation of absolute binding free energies. Proc. Natl. Acad.
Sci. USA (In press) Manas, E., W. Wright, K.A. Sharp, J. Friedrich and J.A. Vanderkooi (2000) The influence of protein environment on the low temperature electronic spectroscopy of Zn substituted cytochrome c. J. Phys. Chem. 104:6932-6941. Chin, K., K.A. Sharp, B. Honig
and A. Pyle (1999) Calculating electrostatic potentials of RNA: providing
new insights into molecular interactions and function. Nature Struct.
Biol. 6:1055-1061. Kuntz, I.D., K. Chen, K.A. Sharp and P. Kollman (1999) The maximal affinity of ligands. Proc. Natl. Acad. Sci. USA 96:9997-10002. Gallagher, K. and K.A. Sharp
(1998) Electrostatic contributions to heat capacity Changes of DNA-ligand
binding. Biophys. J. 75:769-776. Sharp, K.A. and B. Madan (1997) The hydrophobic effect, water structure and heat capacity changes. J. Phys. Chem. 101:4343-48. |
